Paris-DÉCOR: A Protocol for the Determination of Fast Protein Backbone Amide Hydrogen Exchange Rates

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Determining hydrogen exchange kinetics in proteins can shed light on their structure and dynamics. Nuclear magnetic resonance (NMR) spectroscopy is an important analytical technique to determine exchange rates. In this chapter, we describe a new method (Paris-DÉCOR) to determine fast protein amide backbone hydrogen exchange rates in the range 10 to 104 s-1. Measuring fast exchange rates is particularly important for the study of intrinsically disordered proteins, where there is very little protection from exchange to the solvent by the formation of persistent structure. We provide a protocol to set up the experiment as well as MATLAB scripts for numerical simulation that is needed to determine the exchange rates.

Original languageEnglish
Title of host publicationIntrinsically Disordered Proteins
EditorsBirthe B. Kragelund, Karen Skriver
Number of pages8
Place of publicationNew York
PublisherHumana Press
Publication year2020
Pages337-344
ISBN (print)978-1-0716-0523-3
ISBN (Electronic)978-1-0716-0524-0
DOIs
Publication statusPublished - 2020
SeriesMethods in Molecular Biology
Volume2141
ISSN1064-3745

    Research areas

  • Hydrogen exchange, Intrinsically disordered proteins, NMR, Proteins, Spin-spin decorrelation

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